scholarly journals Dissecting the Seed Maturation and Germination Processes in the Non-Orthodox Quercus ilex Species Based on Protein Signatures as Revealed by 2-DE Coupled to MALDI-TOF/TOF Proteomics Strategy

2020 ◽  
Vol 21 (14) ◽  
pp. 4870 ◽  
Author(s):  
Besma Sghaier-Hammami ◽  
Sofiene B.M. Hammami ◽  
Narjes Baazaoui ◽  
Consuelo Gómez-Díaz ◽  
Jesús V. Jorrín-Novo
Keyword(s):  
Amino Acid ◽  
Gel Electrophoresis ◽  
Quercus Ilex ◽  
Developmental Stages ◽  
Tricarboxylic Acid Cycle ◽  
Seed Maturation ◽  
Embryo Axis ◽  
Two Dimensional Gel Electrophoresis ◽  
Cell Defense ◽  
Maldi Tof

Unlike orthodox species, seed recalcitrance is poorly understood, especially at the molecular level. In this regard, seed maturation and germination were studied in the non-orthodox Quercus ilex by using a proteomics strategy based on two-dimensional gel electrophoresis coupled to matrix-assisted laser desorption ionization/time of flight (2-DE-MALDI-TOF).Cotyledons and embryo/radicle were sampled at different developmental stages, including early (M1–M3), middle (M4–M7), and late (M8–M9) seed maturation, and early (G1–G3) and late (G4–G5) germination. Samples corresponding to non-germinating, inviable, seeds were also included. Protein extracts were subjected to 2-dimensional gel electrophoresis (2-DE) and changes in the protein profiles were analyzed. Identified variable proteins were grouped according to their function, being the energy, carbohydrate, lipid, and amino acid metabolisms, together with protein fate, redox homeostasis, and response to stress are the most represented groups. Beyond the visual aspect, morphometry, weight, and water content, each stage had a specific protein signature. Clear tendencies for the different protein groups throughout the maturation and germination stages were observed for, respectively, cotyledon and the embryo axis. Proteins related to metabolism, translation, legumins, proteases, proteasome, and those stress related were less abundant in non-germinating seeds, it related to the loss of viability. Cotyledons were enriched with reserve proteins and protein-degrading enzymes, while the embryo axis was enriched with proteins of cell defense and rescue, including heat-shock proteins (HSPs) and antioxidants. The peaks of enzyme proteins occurred at the middle stages (M6–M7) in cotyledons and at late ones (M8–M9) in the embryo axis. Unlike orthodox seeds, proteins associated with glycolysis, tricarboxylic acid cycle, carbohydrate, amino acid and lipid metabolism are present at high levels in the mature seed and were maintained throughout the germination stages. The lack of desiccation tolerance in Q. ilex seeds may be associated with the repression of some genes, late embryogenesis abundant proteins being one of the candidates.

Accumulation Pattern of Arachin in Maturing Peanut Seed1

1989 ◽  
Vol 16 (2) ◽  
pp. 70-73 ◽  
Author(s):  
Sheikh M. Basha
Keyword(s):  
Amino Acid ◽  
Gel Electrophoresis ◽  
Gel Filtration ◽  
Seed Maturation ◽  
Peanut Seed ◽  
Two Dimensional Gel Electrophoresis ◽  
Accumulation Pattern ◽  
Molecular Weights ◽  
Arachis Hypogaea L ◽  
Compositional Changes

Abstract Accumulation pattern and compositional changes in peanut (Arachis hypogaea L. cv. Florunner) arachin were determined by monitoring arachin from seeds of different maturities by gel filtration, two dimensional gel electrophoresis and amino acid analysis. The results indicated that arachin deposition was maximum between Immature and Intermediate stages, and that the arachin monomer increased more than the polymer during seed maturation. Arachin polypeptides with apparent molecular weights of 70,000: 32,000 and 29,000 increased in abundance with increasing maturity while a 50,000 molecular weight polypeptide decreased during seed maturation. In addition, amino acid composition of arachin differed in seeds of different maturities. These data suggest that arachin polypeptides are not deposited in equal amounts but individual polypeptides accumulate in different proportions during peanut seed maturation.

Separation and Identification of Rice Prolamins by Two-Dimensional Gel Electrophoresis and Amino Acid Sequencing

2012 ◽  
Vol 76 (3) ◽  
pp. 594-597 ◽  
Author(s):  
Takanari SHIGEMITSU ◽  
Yuhi SAITO ◽  
Shigeto MORITA ◽  
Shigeru SATOH ◽  
Takehiro MASUMURA
Keyword(s):  
Amino Acid ◽  
Gel Electrophoresis ◽  
Two Dimensional ◽  
Amino Acid Sequencing ◽  
Two Dimensional Gel Electrophoresis

scholarly journals External scaffold of spherical immature poxvirus particles is made of protein trimers, forming a honeycomb lattice

2005 ◽  
Vol 170 (6) ◽  
pp. 971-981 ◽  
Author(s):  
Patricia Szajner ◽  
Andrea S. Weisberg ◽  
Jacob Lebowitz ◽  
John Heuser ◽  
Bernard Moss
Keyword(s):  
Electron Microscopy ◽  
Amino Acid ◽  
Vaccinia Virus ◽  
Gel Electrophoresis ◽  
Developmental Stages ◽  
Honeycomb Lattice ◽  
Icosahedral Symmetry ◽  
Structural Requirements ◽  
Virus Particles ◽  
Protein Coat

During morphogenesis, poxviruses undergo a remarkable transition from spherical immature forms to brick-shaped infectious particles lacking helical or icosahedral symmetry. In this study, we show that the transitory honeycomb lattice coating the lipoprotein membrane of immature vaccinia virus particles is formed from trimers of a 62-kD protein encoded by the viral D13L gene. Deep-etch electron microscopy demonstrated that anti-D13 antibodies bound to the external protein coat and that lattice fragments were in affinity-purified D13 preparations. Soluble D13 appeared mostly trimeric by gel electrophoresis and ultracentrifugation, which is consistent with structural requirements for a honeycomb. In the presence or absence of other virion proteins, a mutated D13 with one amino acid substitution formed stacks of membrane-unassociated flat sheets that closely resembled the curved honeycombs of immature virions except for the absence of pentagonal facets. A homologous domain that is present in D13 and capsid proteins of certain other lipid-containing viruses support the idea that the developmental stages of poxviruses reflect their evolution from an icosahedral ancestor.

Partial characterization of chromosomal proteins tightly bound to chicken erythroid DNA

1985 ◽  
Vol 63 (8) ◽  
pp. 824-829
Author(s):  
C. C. Liew ◽  
Peter C. Hentzen ◽  
Isaac Bekhor
Keyword(s):  
Amino Acid ◽  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Basic Amino Acid ◽  
Two Dimensional ◽  
Amino Acid Residues ◽  
Two Dimensional Gel Electrophoresis ◽  
Total Dna ◽  
Chromatin Proteins

Extraction of chicken reticulocyte and erythrocyte chromatins with 2 M NaCl yields a small fraction (about 5%) of the total DNA which is very tightly bound to a class of nonhistone chromatin proteins (DNA–P). This DNA fraction has previously been shown to be significantly enriched in active gene sequences. The proteins associated with reticulocyte and erythrocyte DNA–P were analyzed by two-dimensional gel electrophoresis. Reticulocyte DNA–P yield predominantly three major proteins, designated G1, G2, and G3 with relative masses of 80 000, 50 000, and 58 000, respectively. Erythrocyte DNA–P show only two proteins which appear to be similar to the reticulocyte G1 and G2 proteins, except in much reduced quantities as revealed by two-dimensional polyacrylamide gel electrophoresis. Amino acid analysis of the three reticulocyte proteins revealed that the ratio of acidic to basic amino acid residues increased in the order G1 < G2 < G3, while the respective isoelectric points also increased in that order.

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